Glucokinase is a liver enzyme with a kcat of 33/second and a Km
for Glucose of 7 mM. What is the initial reaction rate (in mM
product / second) of 0.1 mM glucokinase in the presence of 50 mM
glucose?
Please show your work clearly.

Glucokinase is a liver enzyme with a kcat of 33/second and a Km for Glucose of...
A dimeric enzyme, glucokinase, has a binding site for glucose in each subunit. The KD for the fi rst binding event is 1 mM and the KD for the second event is 10 μM. a. What is the Hill coefficient? b. Is this protein positively or negatively cooperative with respect to glucose binding
54. What is the catalyze reaction rate? Km=2 mM Kcat= 3 s-1 At the enzyme concentration=10 nM and substrate concentration= 3 mM
An enzyme that follows Michaelis-Menten kinetics has a KM value of 20.0 μM and a kcat value of 211 s−1. At an initial enzyme concentration of 0.0100 μM, the initial reaction velocity was found to be 1.07×10−6 μM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures.
2 (10 marks)The KM and kcat of a carboxypeptidase isoform were found to be 2.00mM and 150s-1 respectively for substrate A. What is the initial rate of the reaction if [A] = 4.00mM and [E]total = 0.010 mM? The presence of a competitive inhibitor [I] = 5.00mM decreases the initial rate by a factor of 2, what is KI?
Values for an Enzyme and a substrate are: Km=4 uM and kcat=20/min. For an experiment where [S]=6mM, it was found that Vo=480nM/min. What was the enzyme concentration? Give your answer in nM. Using the same kcat and Km as the previous question, if [Et]=0.5uM gives a Vo=5 uM/min, what wat the [S]? Give your answer in uM. reaction is run with the kcat=20/min and the Km=4uM. Use the enzyme concentration from question 1 above. A very strong inhibitor is added creating...
3. The enzyme that catalyzes the hydration of CO2 to H2CO3 has a Km = 12 mM and a initial speed of 4.5 micromol formed of H2CO3 / mL per second when [CO2] = 36 mM. a) What is vmax for this enzyme? b) Assuming that 5 pmol / mL (5 x 10-12 mol / mL) of the enzyme was used in the experiment, what is kcat for the enzyme? c) What is the catalytic efficiency of the enzyme? d)...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
Part A An enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 uM and a kcat value of 201 s-1. At an initial enzyme concentration of 0.0100 uM, the initial reaction velocity was found to be 1.07 x 10- uM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures. ► View Available Hint(s) PO ALO O O ? [S]; = MM UM
Given the enzyme system just described (Km = 8.20*10-5M and kcat = 40.0 s-1, [Eltot = 2.00*10-7 M), suppose we introduce a classical noncompetitive inhibitor with K1 = 1.20*10-7M. If the concentration of inhibitor introduced is 3.0 um, what will the effective kcat be? Express your answer in s-1.
included proper units when HLLL 1. The following kinetic data were generated for the enzyme SpB1, this enzyme has an unknown biological function. Using the information provided below answer questions la-le. All reactions had 0.1 mg/mL SPBT which based on amino acid sequence and gel filtration column chromatography has a molecular weight of 42,500 Daltons. S002- Substrate 1 Substrate 2 KM (MM) kcat (sec) glucose >50 <0.01 glucose NADP 4+1 0.5+0.07 glucose NAD 2718 2 +0.05 galactose >50 <0.01 galactose...